Dynamic arrest and aging of biomolecular condensates are modulated by low-complexity domains, RNA and biochemical activity

Miriam Linsenmeier, Maria Hondele, Fulvio Grigolato, Eleonora Secchi, Karsten Weis () and Paolo Arosio ()
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Miriam Linsenmeier: Institute for Chemical and Bioengineering, Swiss Federal Institute of Technology
Maria Hondele: Institute for Biochemistry, Swiss Federal Institute of Technology
Fulvio Grigolato: Institute for Chemical and Bioengineering, Swiss Federal Institute of Technology
Eleonora Secchi: Swiss Federal Institute of Technology
Karsten Weis: Institute for Biochemistry, Swiss Federal Institute of Technology
Paolo Arosio: Institute for Chemical and Bioengineering, Swiss Federal Institute of Technology

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: Abstract Biomolecular condensates require suitable control of material properties for their function. Here we apply Differential Dynamic Microscopy (DDM) to probe the material properties of an in vitro model of processing bodies consisting of out-of-equilibrium condensates formed by the DEAD-box ATPase Dhh1 in the presence of ATP and RNA. By applying this single-droplet technique we show that condensates within the same population exhibit a distribution of material properties, which are regulated on several levels. Removal of the low-complexity domains (LCDs) of the protein decreases the fluidity of the condensates. Structured RNA leads to a larger fraction of dynamically arrested condensates with respect to unstructured polyuridylic acid (polyU). Promotion of the enzymatic ATPase activity of Dhh1 reduces aging of the condensates and the formation of arrested structures, indicating that biochemical activity and material turnover can maintain fluid-like properties over time.

Date: 2022
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DOI: 10.1038/s41467-022-30521-2

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